BARD1 codes for a protein that forms a functional heterodimer with the breast cancer predisposition gene product BRCA1. The BRCA1-BARD1 complex has E3 ubiquitin ligase activity, but not the respective monomers. The specific targets of the BRCA1-BARD1 ubiquitin ligase partially explain the tumor suppressor functions of BARD1 and BRCA1. BRCA1-independent functions are attributed to BARD1, based on its role as inducer of p53-dependent apoptosis. Cancer cells and human cytotrophoblasts express isoforms of BARD1 that lack various functional regions, are void of tumor suppressor functions, and have tumor promoting activities (Irminger-Finger et al. 2015).
The tumor suppressor BARD1 was originally identified as a protein binding to the BRCA1 gene product, BRCA1. The stability of both proteins depends on their interaction via their N-terminal RING finger domains. BRCA1 depends on binding to BARD1 for...
KeywordsRing Finger Tumor Suppressor Function Differential Splice Ubiquitin Ligase Activity Ring Finger Domain
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